The heats of reaction of trypsin with soybean (Kunitz), ovomucoid, and lima bean inhibitors have been measured at pH 5.0 and 10’ and 25”. All the reactions were endothermic, with AH ranging from 8.6 Cal per mole for the lima bean inhibitor to 15.3 Cal per mole for the soybean inhibitor. Equilibrium constants for the association were calculated from the dependence of residual tryptic activity up...

Dissociation of mixed trypsin (bovine plus porcine trypsin) complexes with chicken ovoinhibitor was used to investigate the nonequivalence of the two binding sites for trypsin on the inhibitor. Previous work has shown that 1 mol of trypsin dissociates much more rapidly than the 2nd from unmixed trypsin complexes, those containing 2 mol of one kind of trypsin, bovine or porcine, per mol of inhib...

Protein hydrolysate is highly regarded as a source of naturally occurring antioxidant peptides. The purpose of this study was to investigate the effect of Ultrasonic (Frequency, 20 KHz; Amplitude, 50%; Time, 30 min) and high-pressure homogenization (Power, 1500 bar; Rated flow, 10 dm/h) pretreatmenton the enzymatic hydrolysis and antioxidant properties of yeast protein hydrolysate obtained from...

Trypsin inhibitors are proteins found in plant-based foods, mainly legumes and cereals. They have traditionally been described as anti-nutrients since their consumption leads to lower protein digestibility along with pancreatic hypertrophy. Given the problems which can arise, there various technologies used food processing help reduce trypsin safe levels. It has also that be related beneficial ...